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Magnesium in PDB 1rev: Hiv-1 Reverse Transcriptase

Enzymatic activity of Hiv-1 Reverse Transcriptase

All present enzymatic activity of Hiv-1 Reverse Transcriptase:
2.7.7.49;

Protein crystallography data

The structure of Hiv-1 Reverse Transcriptase, PDB code: 1rev was solved by J.Ren, R.Esnouf, A.Hopkins, C.Ross, Y.Jones, D.Stammers, D.Stuart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 138.800, 115.800, 66.200, 90.00, 90.00, 90.00
R / Rfree (%) 22.4 / n/a

Other elements in 1rev:

The structure of Hiv-1 Reverse Transcriptase also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Hiv-1 Reverse Transcriptase (pdb code 1rev). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Hiv-1 Reverse Transcriptase, PDB code: 1rev:

Magnesium binding site 1 out of 1 in 1rev

Go back to Magnesium Binding Sites List in 1rev
Magnesium binding site 1 out of 1 in the Hiv-1 Reverse Transcriptase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Hiv-1 Reverse Transcriptase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1000

b:53.2
occ:1.00
OD2 A:ASP443 2.6 82.5 1.0
O A:HOH1108 2.6 59.5 1.0
O A:VAL442 3.2 65.3 1.0
CG A:ASP443 3.7 77.0 1.0
OD1 A:ASP443 4.3 71.2 1.0
CB A:ALA538 4.3 0.0 1.0
C A:VAL442 4.4 62.5 1.0
CB A:TYR441 4.6 52.8 1.0
CG2 A:VAL536 4.6 65.8 1.0
CD2 A:TYR441 4.6 39.4 1.0
O A:VAL496 4.7 39.7 1.0
C A:TYR441 4.7 55.1 1.0
N A:VAL442 4.8 59.2 1.0
CG1 A:VAL496 4.8 25.4 1.0
CB A:ASP443 4.9 72.1 1.0
CA A:TYR441 4.9 50.1 1.0
CB A:ASP498 5.0 59.9 1.0

Reference:

J.Ren, R.Esnouf, A.Hopkins, C.Ross, Y.Jones, D.Stammers, D.Stuart. The Structure of Hiv-1 Reverse Transcriptase Complexed with 9-Chloro-Tibo: Lessons For Inhibitor Design. Structure V. 3 915 1995.
ISSN: ISSN 0969-2126
PubMed: 8535785
DOI: 10.1016/S0969-2126(01)00226-X
Page generated: Tue Aug 13 12:59:27 2024

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